Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending.

Autor:	Hu Y; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Schwab S; Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333CC Leiden, The Netherlands; Centre for Microbial Cell Biology, Leiden University, Leiden, The Netherlands; Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands., Deiss S; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Escudeiro P; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., van Heesch T; Van 't Hoff Institute for Molecular Sciences, University of Amsterdam, The Netherlands., Joiner JD; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Vreede J; Van 't Hoff Institute for Molecular Sciences, University of Amsterdam, The Netherlands., Hartmann MD; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany.; Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany., Lupas AN; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Alvarez BH; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Alva V; Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany., Dame RT; Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333CC Leiden, The Netherlands; Centre for Microbial Cell Biology, Leiden University, Leiden, The Netherlands; Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2024 Aug 12; Vol. 52 (14), pp. 8193-8204.
DOI:	10.1093/nar/gkae485
Abstrakt:	Histones are essential for genome compaction and transcription regulation in eukaryotes, where they assemble into octamers to form the nucleosome core. In contrast, archaeal histones assemble into dimers that form hypernucleosomes upon DNA binding. Although histone homologs have been identified in bacteria recently, their DNA-binding characteristics remain largely unexplored. Our study reveals that the bacterial histone HBb (Bd0055) is indispensable for the survival of Bdellovibrio bacteriovorus, suggesting critical roles in DNA organization and gene regulation. By determining crystal structures of free and DNA-bound HBb, we unveil its distinctive dimeric assembly, diverging from those of eukaryotic and archaeal histones, while also elucidating how it binds and bends DNA through interaction interfaces reminiscent of eukaryotic and archaeal histones. Building on this, by employing various biophysical and biochemical approaches, we further substantiated the ability of HBb to bind and compact DNA by bending in a sequence-independent manner. Finally, using DNA affinity purification and sequencing, we reveal that HBb binds along the entire genomic DNA of B. bacteriovorus without sequence specificity. These distinct DNA-binding properties of bacterial histones, showcasing remarkable similarities yet significant differences from their archaeal and eukaryotic counterparts, highlight the diverse roles histones play in DNA organization across all domains of life. (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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